HMM Summary Page: TIGR00285
| Accession | TIGR00285 |
| Name | TIGR00285 |
| Function | DNA-binding protein Alba |
| Gene Symbol | albA |
| Trusted Cutoff | 88.25 |
| Domain Trusted Cutoff | 88.25 |
| Noise Cutoff | 26.25 |
| Domain Noise Cutoff | 26.25 |
| Isology Type | equivalog |
| HMM Length | 87 |
| Mainrole Category | DNA metabolism |
| Subrole Category | Chromosome-associated proteins |
| Gene Ontology Term | GO:0003677: DNA binding molecular_function |
| GO:0006325: chromatin organization biological_process | |
| Author | Haft DH, Dodson RJ |
| Entry Date | Apr 20 1999 2:05PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Alba has been shown to bind DNA and affect DNA supercoiling in a temperature dependent manner. It is regulated by acetylation (alba = acetylation lowers binding affinity) by the Sir2 protein. Alba is proposed to play a role in establishment or maintenace of chromatin architecture and thereby in transcription repression. This protein appears so far only in the Archaea, but may be universal there. There is a single member in three of the first four completed archaeal genomes, and a second copy in A. fulgidus. In Sulfolobus shibatae there is a tandem second copy that is poorly conserved and scores below the trusted cutoff; all other members of the family are conserved at greater than 50 % pairwise identity. |
| References | [1] RM 10869069 RT An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion. RL J Bacteriol. 2000 Jul;182(14):3929-33. RA Xue H, Guo R, Wen Y, Liu D, Huang L. [2] RM 11935028 RT The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. RL Science. 2002 Apr 5;296(5565):148-51. RA Bell SD, Botting CH, Wardleworth BN, Jackson SP, White MF. SE TIGR GA hmmls AL clustalw, belvu DR HAMAP; MF_01122; 29 of 33 |